HDAC9
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Histone deacetylase 9 is an enzyme that in humans is encoded by the HDAC9 gene.[5][6][7]
Function
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.[7]
Interactions
HDAC9 has been shown to interact with:
See also
References
- ↑ "Diseases that are genetically associated with HDAC9 view/edit references on wikidata".
- ↑ "Drugs that physically interact with Histone deacetylase 9 view/edit references on wikidata".
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ (November 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Mol Cell Biol. 19 (11): 7816–27. doi:10.1128/mcb.19.11.7816. PMC 84849
. PMID 10523670. - ↑ Sparrow DB, Miska EA, Langley E, Reynaud-Deonauth S, Kotecha S, Towers N, Spohr G, Kouzarides T, Mohun TJ (November 1999). "MEF-2 function is modified by a novel co-repressor, MITR". EMBO J. 18 (18): 5085–98. doi:10.1093/emboj/18.18.5085. PMC 1171579. PMID 10487760.
- 1 2 "Entrez Gene: HDAC9 histone deacetylase 9".
- 1 2 Zhang CL, McKinsey TA, Olson EN (October 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/mcb.22.20.7302-7312.2002. PMC 139799. PMID 12242305.
- 1 2 3 Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A (May 2003). "The histone deacetylase 9 gene encodes multiple protein isoforms". J. Biol. Chem. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135.
- ↑ Zhou X, Richon VM, Rifkind RA, Marks PA (February 2000). "Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5". Proc. Natl. Acad. Sci. U.S.A. 97 (3): 1056–61. doi:10.1073/pnas.97.3.1056. PMC 15519. PMID 10655483.
- ↑ Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (September 1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". EMBO J. 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. PMC 1171580. PMID 10487761.
- ↑ Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S (May 2000). "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity". J. Biol. Chem. 275 (20): 15594–9. doi:10.1074/jbc.M908437199. PMID 10748098.
- ↑ Koipally J, Georgopoulos K (June 2002). "Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression". J. Biol. Chem. 277 (26): 23143–9. doi:10.1074/jbc.M202079200. PMID 11959865.
Further reading
- Marks PA, Richon VM, Rifkind RA (2000). "Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells.". J. Natl. Cancer Inst. 92 (15): 1210–6. doi:10.1093/jnci/92.15.1210. PMID 10922406.
- Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators.". Trends Genet. 19 (5): 286–93. doi:10.1016/S0168-9525(03)00073-8. PMID 12711221.
- "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1999). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
- Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor.". EMBO J. 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. PMC 1171580. PMID 10487761.
- Zhou X, Richon VM, Rifkind RA, Marks PA (2000). "Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5.". Proc. Natl. Acad. Sci. U.S.A. 97 (3): 1056–61. doi:10.1073/pnas.97.3.1056. PMC 15519. PMID 10655483.
- Youn HD, Grozinger CM, Liu JO (2000). "Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4.". J. Biol. Chem. 275 (29): 22563–7. doi:10.1074/jbc.C000304200. PMID 10825153.
- Zhang CL, McKinsey TA, Lu JR, Olson EN (2001). "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor.". J. Biol. Chem. 276 (1): 35–9. doi:10.1074/jbc.M007364200. PMID 11022042.
- Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E (2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo.". J. Biol. Chem. 276 (38): 35826–35. doi:10.1074/jbc.M104935200. PMID 11466315.
- Zhou X, Marks PA, Rifkind RA, Richon VM (2001). "Cloning and characterization of a histone deacetylase, HDAC9.". Proc. Natl. Acad. Sci. U.S.A. 98 (19): 10572–7. doi:10.1073/pnas.191375098. PMC 58507. PMID 11535832.
- Koipally J, Georgopoulos K (2002). "Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression.". J. Biol. Chem. 277 (26): 23143–9. doi:10.1074/jbc.M202079200. PMID 11959865.
- Kirsh O, Seeler JS, Pichler A, Gast A, Müller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A (2002). "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.". EMBO J. 21 (11): 2682–91. doi:10.1093/emboj/21.11.2682. PMC 125385. PMID 12032081.
- Mahlknecht U, Schnittger S, Will J, Cicek N, Hoelzer D (2002). "Chromosomal organization and localization of the human histone deacetylase 9 gene (HDAC9).". Biochem. Biophys. Res. Commun. 293 (1): 182–91. doi:10.1016/S0006-291X(02)00193-6. PMID 12054582.
- Zhang CL, McKinsey TA, Olson EN (2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation.". Mol. Cell. Biol. 22 (20): 7302–12. doi:10.1128/MCB.22.20.7302-7312.2002. PMC 139799. PMID 12242305.
- Hoogeveen AT, Rossetti S, Stoyanova V, Schonkeren J, Fenaroli A, Schiaffonati L, van Unen L, Sacchi N (2002). "The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies.". Oncogene. 21 (43): 6703–12. doi:10.1038/sj.onc.1205882. PMID 12242670.
- Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A (2003). "The histone deacetylase 9 gene encodes multiple protein isoforms.". J. Biol. Chem. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135.
External links
- HDAC9 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
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